Structural exploration of antibacterial activity and hemolytic profiles of non-natural analogs of the antimicrobial peptide mastoparan mp-8

In this work the relevance of a systematic replacement of peptide-bonds on the Mastoparan MP-8 antimicrobial peptide to afford 27 new pseudopeptide analogues is reported. Results allowed to determine that pseudopeptides ψ-38617 (INLKALAALAKd-[CH2NH]-RLL), ψ-38629(INLKAd-[CH2NH]-LAALAKRLL) and ψ-38630 (INLK-[CH2NH]-ALAALAKRLL), showed an enhanced anti gam-negative bacterial properties, regarding the native Mastoparan MP-8 peptide, but maintaining a comparable activity against gram-positive bacteria. In addition, specific performed modifications on MP-8 sequence led three new molecules that completely abolished the hemolytic activity of the parent MP-8 peptide. All obtained molecules possess a high stability profile when tested against a severe proteolytic attack.

• Autores: Carreño, Luisa Fernanda; Lozano, José Manuel
• Tipo de recurso: Article of journal
• Fecha de publicación: 2013
• Institución: Universidad Nacional de Colombia
• Repositorio: Universidad Nacional de Colombia
• Idioma: spa
• OAI Identifier: oai:repositorio.unal.edu.co:unal/49320
• Acceso en línea: https://repositorio.unal.edu.co/handle/unal/49320; http://bdigital.unal.edu.co/42777/; http://bdigital.unal.edu.co/42777/2/
• Palabra clave: péptido antimicrobiano; Mastoparán MP-8; actividad hemolítica; estabilidad; antimicrobial peptide; Mastoparan MP-8; hemolytic activity; stability
• Rights: openAccess
• License: Atribución-NoComercial 4.0 Internacional